The DOI matches its Crossref record; 150 of the 152 references it cites were found in a registry or an index.
Macrophages and Iron Metabolism
Open accessAbstract
Iron is a transition metal that due to its inherent ability to exchange electrons with a variety of molecules is essential to support life. In mammals, iron exists mostly in the form of heme, enclosed within an organic protoporphyrin ring and functioning primarily as a prosthetic group in proteins. Paradoxically, free iron also has the potential to become cytotoxic when electron exchange with oxygen is unrestricted and catalyzes the production of reactive oxygen species. These biological properties demand that iron metabolism is tightly regulated such that iron is available for core biological functions while preventing its cytotoxic effects. Macrophages play a central role in establishing this delicate balance. Here, we review the impact of macrophages on heme-iron metabolism and, reciprocally, how heme-iron modulates macrophage function.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Macrophage plays a central role in iron metabolism, including heme-iron turnover in senescent red blood cells, hepcidin regulation and lipocalin system [68].”
From Asbestos conceives Fe(II)-dependent mutagenic stromal milieu through ceaseless macrophage ferroptosis and β-catenin induction in mesothelium (2020) · cites this paper as [68]
Experimental — accuracy not yet measuredIn the citing paper
“Second, the degradation of Bach1 induces expression of the transcription factor (an E26 transformation-specific transcription factor of the Spi subfamily) SpiC independently of Nrf2 [116, 211].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [211]
In the citing paper
“This is circumvented by the recycling of the Fe contained in the heme groups of Hb inside RBC (14–16), achieved largely via the continuous engulfment and digestion of senescent or damaged RBC by erythrophagocytic macrophages (EM) in the red pulp of the spleen (15) (Figure 1).”
From Innate Nutritional Immunity (2018) · cites this paper as [15]
In the citing paper
“This process allows for the Fe contained in the heme groups of Hb to be extracted and directed into the bone marrow to support erythropoiesis, where Fe is inserted in the last step of heme biosynthesis and incorporated into nascent Hb (15) (Figure 1).”
From Innate Nutritional Immunity (2018) · cites this paper as [15]
In the citing paper
“In addition, pathogen sensing via PRRs promotes resistance mechanisms in innate immune cells, which withhold heme-Fe from pathogens (15) (Figure 3).”
From Innate Nutritional Immunity (2018) · cites this paper as [15]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Ferroptosis: An Iron-Dependent Form of Nonapoptotic Cell Death
Dixon, S. J., Lemberg, K. M., Lamprecht, M. R., Skouta, R., Zaitsev, E. M., Gleason, C. E., Patel, D. N., Bauer, A. J., Cantley, A. M., Yang, W. S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.042 · Cited by 18,691
Janeway, C. A., & Medzhitov, R. (2002) · Annual Review of Immunology · doi:10.1146/annurev.immunol.20.083001.084359 · Cited by 8,394
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
Origin and physiological roles of inflammation
Medzhitov, R. (2008) · Nature · doi:10.1038/nature07201 · Cited by 6,618
Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly
Beckman, J. S., & Koppenol, W. H. (1996) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1996.271.5.c1424 · Cited by 5,513
Macrophage biology in development, homeostasis and disease
Wynn, T. A., Chawla, A., & Pollard, J. W. (2013) · Nature · doi:10.1038/nature12034 · Cited by 4,684 · cited 2×
“However, intracellular iron also downregulates NOS2 transcription in response to IFN-g (Weiss et al., 1992) via a mechanism involving STAT inhibition (Xie et al., 1994).”
BackgroundHypoxia-inducible factors in physiology and medicine
Semenza, G. L. (2012) · Cell · doi:10.1016/j.cell.2012.01.021 · Cited by 3,645
Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630
Targeting the KEAP1-NRF2 system to prevent kidney disease progression
Nezu, M., Suzuki, N., & Yamamoto, M. (2017) · American Journal of Nephrology · doi:10.1159/000475890 · Cited by 3,447
Cited by
Sorted by citations
Items 201–300 of 402
O′Neill, E., Mela, V., Gaban, A. S., Béchet, S., McGrath, A., Walsh, A., McIntosh, A. L., & Lynch, M. A. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.939830 · Cited by 17
Interleukin-10 attenuates renal injury after myocardial infarction in diabetes
Fan, X., Zhang, X., Liu, L., Kim, A. Y., Curley, S. P., Chen, X., Dworkin, L. D., Cooper, C. J., & Gupta, R. (2022) · Journal of Investigative Medicine · doi:10.1136/jim-2021-002008 · Cited by 16
The role of macrophage polarization and function in environmental toxicant-induced cancers
Sepand, M. R., Aghsami, M., Keshvadi, M., Bigdelou, B., Behzad, R., Zanganeh, S., & Shadboorestan, A. (2021) · Environmental Research · doi:10.1016/j.envres.2021.110933 · Cited by 16
Imoto, S., Sawamura, T., Shibuya, Y., Kono, M., Ohbuchi, A., Suzuki, T., Mizokoshi, Y., & Saigo, K. (2021) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2021.103319 · Cited by 16
Sperry, M. M., Novak, R., Keshari, V., Dinis, A., Cartwright, M. J., Camacho, D. M., Paré, J., Super, M., Levin, M. G., & Ingber, D. E. (2022) · Advanced Science · doi:10.1002/advs.202200222 · Cited by 13
Doan, L. H., Chu, L.-W., Huang, Z.-Y., Nguyen, A. T., Lee, C., Huang, C., Chang, Y.-F., Hsieh, W.-Y., Nguyen, T. T. H., Lin, C., et al. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.905197 · Cited by 15
Cui, Y., Gutiérrez, S., Ariai, S., Öberg, L., Thörn, K., Gehrmann, U., Cloonan, S. M., Naessens, T., & Olsson, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.998059 · Cited by 16
Li, J., Liu, L., Xing, J., Chen, D., Fang, C., Mo, F., Gong, Y., Tan, Z., Liang, G., Xiao, W. L., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1123074 · Cited by 15
Critical Role for Molecular Iron in Coxiella burnetii Replication and Viability
Sanchez, S. E., & Omsland, A. (2020) · mSphere · doi:10.1128/msphere.00458-20 · Cited by 15
Ironing out the distribution of [2Fe-2S] motifs in ferrochelatases
Weerth, R. S., Medlock, A. E., & Dailey, H. A. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101017 · Cited by 15
Acute Hemolysis and Heme Suppress Anti-CD40 Antibody-Induced Necro-Inflammatory Liver Disease
Pfefferlé, M., Ingoglia, G., Schaer, C. A., Hansen, K., Schulthess, N., Humar, R., Schaer, D. J., & Vallelian, F. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.680855 · Cited by 16
Intracellular growth of Brucella is mediated by Dps‐dependent activation of ferritinophagy
Hop, H. T., Huy, T. X. N., Lee, H.-J., & Kim, S. (2023) · EMBO Reports · doi:10.15252/embr.202255376 · Cited by 15
Iron: The silent culprit in your adipose tissue
Moreno‐Navarrete, J. M., & Fernández‐Real, J. M. (2023) · Obesity Reviews · doi:10.1111/obr.13647 · Cited by 15
Access and utilization of host-derived iron by Leishmania parasites
Goto, Y., Ito, T., Ghosh, S., & Mukherjee, B. (2023) · The Journal of Biochemistry · doi:10.1093/jb/mvad082 · Cited by 14
Schaefer, R. E. M., Callahan, R. C., Atif, S. M., Orlicky, D. J., Cartwright, I. M., Fontenot, A. P., Colgan, S. P., & Onyiah, J. C. (2021) · Mucosal Immunology · doi:10.1038/s41385-021-00474-8 · Cited by 14
Associations of metal profiles in blood with thyroiditis: a cross-sectional study
Luo, Y., Zeng, H., Ye, Y., Yu, G., Song, C., Liu, S. M., Chen, X., Jiang, Y., Duan, H., Li, Y., et al. (2022) · Environmental Science and Pollution Research · doi:10.1007/s11356-022-23625-1 · Cited by 14
Iron in blood cells: Function, relation to disease, and potential for magnetic separation
Barua, S., Ciannella, S., Tijani, L., & Gómez‐Pastora, J. (2023) · Biotechnology and Bioengineering · doi:10.1002/bit.28388 · Cited by 16
Jakubowska, M. A., Pyka, J., Michalczyk‐Wetula, D., Baczyński, K., Cieśla, M., Susz, A., Ferdek, P. E., Płonka, B. K., Fiedor, L., & Plonka, P. M. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101566 · Cited by 14
Zhou, T., Xu, Z., Sun, H., Beltrán, A. M., Nawaz, Q., Sui, B., Boccaccini, A. R., & Zheng, K. (2024) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2024.134188 · Cited by 13
A role for hepcidin in the anemia caused by Trypanosoma brucei infection
Neves, J. V., Gomes, A. C., Costa, D. M., Barroso, C., Vaulont, S., Cordeiro‐da‐Silva, A., Tavares, J., & Rodrigues, P. (2020) · Haematologica · doi:10.3324/haematol.2019.227728 · Cited by 13
Ameka, M., & Hasty, A. H. (2020) · Immunometabolism · doi:10.20900/immunometab20200034 · Cited by 12
Gland Macrophages: Reciprocal Control and Function within Their Niche
Bijnen, M., & Bajénoff, M. (2021) · Trends in Immunology · doi:10.1016/j.it.2020.12.006 · Cited by 14
Padilla, S., Nurden, A. T., do Prado, R. C. P., Nurden, P., & Anitua, E. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121205 · Cited by 15
Gut Dysbiosis: A Target for Protective Interventions against Parkinson’s Disease
Lima, I. S., Pêgo, A. C., Martins, A. C., Prada, A. R., Barros, J. T., Martins, G., & Gozzelino, R. (2023) · Microorganisms · doi:10.3390/microorganisms11040880 · Cited by 15
Gauthier, A. G., Wu, J., Lin, M., Sitapara, R. A., Kulkarni, A., Thakur, G. A., Schmidt, E. E., Perron, J. C., Ashby, C. R., & Mantell, L. L. (2021) · Antioxidants · doi:10.3390/antiox10010135 · Cited by 13
Ferroptosis contributes to immunosuppression
He, N., Yuan, D., Luo, M., Xu, Q., Wen, Z., Wang, Z., Zhao, J., & Liu, Y. (2024) · Frontiers of Medicine · doi:10.1007/s11684-024-1080-8 · Cited by 13
Reviewing the function of macrophages in liver disease
Chen, L., Guillot, A., & Tacke, F. (2025) · Expert Review of Gastroenterology & Hepatology · doi:10.1080/17474124.2025.2508963 · Cited by 15
Challenging patient phenotypes in the management of anaemia of chronic kidney disease
Pramod, S., & Goldfarb, D. S. (2021) · International Journal of Clinical Practice · doi:10.1111/ijcp.14681 · Cited by 11
Nasir, N. J. M., Heemskerk, H., Jenkins, J., Hamadee, N. H., Bunte, R. M., & Tucker‐Kellogg, L. (2023) · eLife · doi:10.7554/elife.85633 · Cited by 11
Askri, D., Ouni, S., Galai, S., Chovelon, B., Arnaud, J., Lehmann, S. G., Sakly, M., Sève, M., & Amara, S. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.06.006 · Cited by 11
Characteristics of macrophages from myelodysplastic syndrome microenvironment
Yang, F., Wu, Z., Yang, D., Zhang, X., Zhang, X., & Xu, Y. (2021) · Experimental Cell Research · doi:10.1016/j.yexcr.2021.112837 · Cited by 11
Imbalanced and Unchecked: The Role of Metal Dyshomeostasis in Driving COPD Progression
Cui, Y., Du, X., Li, Y., Wang, D., Lv, Z., Yuan, H., Chen, Y., Liu, J., Sun, Y., & Wang, W. (2024) · COPD Journal of Chronic Obstructive Pulmonary Disease · doi:10.1080/15412555.2024.2322605 · Cited by 13
Qiu, X., Wang, W.-P., Shen, C., Zhao, Y., Song, X., Yu, Y., Liu, C., Wu, W., Miao, L., & Ren, S. (2025) · Bioactive Materials · doi:10.1016/j.bioactmat.2025.05.009 · Cited by 11
Lissner, M. M., Cumnock, K., Davis, N. M., Vilches-Moure, J. G., Basak, P., Navarrete, D. J., Allen, J. A., & Schneider, D. S. (2020) · eLife · doi:10.7554/elife.60165 · Cited by 13
Inflammatory pathways and anti‐inflammatory therapies in sickle cell disease
Tozatto‐Maio, K., Rós, F. A., Weinlich, R., & Rocha, V. (2024) · HemaSphere · doi:10.1002/hem3.70032 · Cited by 10
Crosstalk Between Sickle Cell Disease and Ferroptosis
Russo, A., Patanè, G. T., Calderaro, A., Barreca, D., Tellone, E., & Putaggio, S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083675 · Cited by 11
Qian, Z., Zhang, Z., Bai, W., Li, J., Rao, X., Huang, G., Liu, J., & Wei, W. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1628142 · Cited by 12
Patidar, A., Malhotra, H., Chaudhary, S., Kumar, M., Dilawari, R., Chaubey, G., Dhiman, A., Modanwal, R., Talukdar, S., Raje, C., et al. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-04110-3 · Cited by 9
Fuhrmann, D. C., Becker, S. A., & Brüne, B. (2022) · FEBS Letters · doi:10.1002/1873-3468.14545 · Cited by 10
Zhang, M., Xiong, W., Qiao, R., Li, M., Zhang, C., Yang, C., Zhu, Y., He, J., & Ma, Z. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1570157 · Cited by 10
Sarkar, A., Andrews, N. W., & Laranjeira‐Silva, M. F. (2019) · International Journal for Parasitology · doi:10.1016/j.ijpara.2019.02.002 · Cited by 9
Pascual-Guàrdia, S., Ferrer, A., Díaz, Ó. D., Caguana-Vélez, O. A., Tejedor, E., Bellido-Calduch, S., Rodriguez, D. A., & Gea, J. (2021) · Archivos de Bronconeumología · doi:10.1016/j.arbr.2021.10.010 · Cited by 9
Ferritin from Mycobacterium abscessus is involved in resistance to antibiotics and oxidative stress
Pereira, M. M. R., de Oliveira, F. M., da Costa, A. C., Junqueira‐Kipnis, A. P., & Kipnis, A. (2023) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12420-8 · Cited by 9
Inorganic ion-sensitive imaging probes for biomedical applications
Wang, Q., Wang, P., Huang, C., Cui, S., Yang, S., Li, F., & Ling, D. (2023) · Chemical Communications · doi:10.1039/d3cc00418j · Cited by 9
Yang, Y., Zhao, M., Kuang, Q.-X., You, F., & Jiang, Y. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.155451 · Cited by 9
Assis‐Mendonça, G. R., Cunha‐Silva, M., Fernandes, M. F., Torres, L. D., Veríssimo, M. P. D. A., Okano, M. T. N., Mazo, D. F. D. C., Lalli, C. A., Sevá‐Pereira, T., Stelini, R. F., et al. (2020) · BMC Gastroenterology · doi:10.1186/s12876-020-01468-9 · Cited by 9
Hijacking Self‐Assembly to Establish Intracellular Functional Nanoparticles
Liu, Y., Wang, Y., Wang, C., Dong, T., Xu, H., Guo, Y., Zhao, X., Hu, Y., & Wu, J. (2022) · Advanced Science · doi:10.1002/advs.202203027 · Cited by 9
Long non-coding RNA SeT and miR-155 regulate the Tnfα gene allelic expression profile
Stathopoulou, C., Kapsetaki, M., Stratigi, K., & Spilianakis, C. G. (2017) · PLoS ONE · doi:10.1371/journal.pone.0184788 · Cited by 9
Ironing-Out the Role of Hepcidin in Atherosclerosis
Guo, L., Sakamoto, A., Cornelissen, A., Hong, C. C., & Finn, A. V. (2019) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.119.312369 · Cited by 9
Paying the Iron Price: Liver Iron Homeostasis and Metabolic Disease
Ameka, M., & Hasty, A. H. (2022) · Comprehensive physiology · doi:10.1002/cphy.c210039 · Cited by 17
Yang, W.-P., Li, M.-Q., Ding, J. M., Li, J., Wu, G., Liu, B., Gao, Y., Wang, G., & Luo, Q. (2024) · eLife · doi:10.7554/elife.87496.4 · Cited by 8
Homeostatic control of energy metabolism by monocyte-derived macrophages
Martins, R., Blankehaus, B., Braza, F., Mesquita, M., Ventura, P., Singh, S., Weis, S., Pires, M. V., Pagnotta, S. E., Wu, Q., et al. (2025) · The EMBO Journal · doi:10.1038/s44318-025-00622-x · Cited by 10
Self-citationActivation of NLRP3 Inflammasome by Virus-Like Particles of Human Polyomaviruses in Macrophages
Lučiūnaitė, A., Dalgėdienė, I., Žilionis, R., Mašalaitė, K., Norkienė, M., Šinkūnas, A., Gedvilaitė, A., Kučinskaitė-Kodzė, I., & Žvirblienė, A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.831815 · Cited by 8
Macrophage vesicles starve bacteria of iron
Weiß, G. (2023) · Nature Metabolism · doi:10.1038/s42255-022-00719-1 · Cited by 8
Volk, K. M., Schleh, M. W., Harrison, F. E., & Hasty, A. H. (2023) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2023.12.020 · Cited by 8
Novel insights into macrophage immunometabolism in nonalcoholic steatohepatitis
Yuan, Y., Zhang, Y., Lu, X., Li, J., Wang, M., Zhang, W., Zheng, M., Sun, Z., Xing, Y., Li, Y., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.111833 · Cited by 8
Puzzling out iron complications in cancer drug resistance
Abedi, M., & Rahgozar, S. (2022) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2022.103772 · Cited by 8
Analyzing the Quenchable Iron Pool in Murine Macrophages by Flow Cytometry
Riedelberger, M., & Kuchler, K. (2020) · BIO-PROTOCOL · doi:10.21769/bioprotoc.3552 · Cited by 8
Brownhill, E., Yabaji, S. M., Zhernovkov, V., Rukhlenko, O. S., Seidel, K., Bhattacharya, B., Chatterjee, S., Chen, H. A., Crossland, N. A., Bishai, W. R., et al. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.14.422743 · Cited by 8
Human skeletal muscle ageing atlasPreprint
Kedlian, V. R., Wang, Y., Liu, T., Chen, X., Bolt, L., Shen, Z., Fasouli, E. S., Prigmore, E., Kleshchevnikov, V., Li, T., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.24.493094 · Cited by 8
Chen, X., Zhi, L.-J., Chen, J., Li, R., & Long, K. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2024.1456535 · Cited by 10
Homing pigeon navigation relies on superparamagnetic macrophages under overcast conditions
Lisowski, C., Quetting, M., Klaus, D., Lazarevski, L., Seep, L., Germer, M., Li, J., Müller, I., Zúñiga, D., Fiedler, W., et al. (2026) · Science · doi:10.1126/science.ady2486 · Cited by 7
Pascual-Guàrdia, S., Ferrer, A., Díaz, Ó. D., Caguana-Vélez, O. A., Tejedor, E., Bellido-Calduch, S., Rodriguez, D. A., & Gea, J. (2021) · Archivos de Bronconeumología · doi:10.1016/j.arbres.2021.03.015 · Cited by 7
Donor-Derived Myeloid Heme Oxygenase-1 Controls the Development of Graft-Versus-Host Disease
Spilleboudt, C., Wilde, V. D., Lewalle, P., Cabanne, L., Leclerc, M., Beckerich, F., Bories, D., Cardoso, S., Soares, M. P., Vokaer, B., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2020.579151 · Cited by 7
Self-citationYang, W.-P., Li, M.-Q., Ding, J. M., Li, J., Wu, G., Liu, B., Gao, Y., Wang, G., & Luo, Q. (2023) · eLife · doi:10.7554/elife.87496 · Cited by 16
Regulation of macrophage iron homeostasis is associated with the localization of bacteria
Gan, Z.-S., Tang, X., Wang, Z., Li, J., Wang, Z., & Du, H. (2018) · Metallomics · doi:10.1039/c8mt00301g · Cited by 7
Xue, Y., Wang, S., Yin, Y., Chai, X., Zhou, Z., Li, H., Mou, H., Wang, F., Yao, M., Zhao, S., et al. (2025) · ACS Nano · doi:10.1021/acsnano.5c11563 · Cited by 7
Heme- and iron-activated macrophages in sickle cell disease: an updated perspective
Navaneethabalakrishnan, S., An, X., & Vinchi, F. (2024) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000836 · Cited by 6
Yang, J., Fu, Q., Jiang, H., Zhong, H., Qin, H., Miao, X., Li, Y., Liu, M., & Yao, J. (2024) · Journal of Photochemistry and Photobiology B Biology · doi:10.1016/j.jphotobiol.2024.113003 · Cited by 6
Rostami, R., Beiranvand, A., Nourooz‐Zadeh, S., Rostami, M., Mohammadi, A., & Nourooz‐Zadeh, J. (2024) · Intern J Endocrinol Metab · doi:10.5812/ijem-145599 · Cited by 6
Maturation of phagosomes containing different erythrophagocytic particles in primary macrophages
Santarino, I. B., & Vieira, O. V. (2017) · FEBS Open Bio · doi:10.1002/2211-5463.12262 · Cited by 6
Imoto, S., Shibuya, Y., Kono, M., Ohbuchi, A., Sawamura, T., Suzuki, T., Mizokoshi, Y., Sawada, H., & Saigo, K. (2019) · Transfusion and Apheresis Science · doi:10.1016/j.transci.2019.10.004 · Cited by 6
Defective iron homeostasis and hematological abnormalities in Niemann-Pick disease type C1
Chen, O. C. W., Siebel, S., Colaço, A., Nicoli, E., Platt, N., Shepherd, D., Newman, S. K., Armitage, A. E., Farhat, N. Y., Seligmann, G., et al. (2022) · Wellcome Open Research · doi:10.12688/wellcomeopenres.17261.1 · Cited by 6
Real-time pH imaging of macrophage lysosomes using the pH-sensitive probe ApHID
Solé‐Domènech, S., Singh, P. K., Funes, L., Ma, C.-I. J., Warren, J. D., & Maxfield, F. R. (2025) · Cell Reports Methods · doi:10.1016/j.crmeth.2025.101203 · Cited by 5
Wang, S., Liu, X., Xu, L., Lang, J., & Liu, D. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1537651 · Cited by 5
Autophagy is involved in Salmonella Typhimurium-induced ferroptosis in macrophages
Liu, W., Fu, D. C., Di, C., Sun, J. F., & Liu, P. (2025) · Veterinary Microbiology · doi:10.1016/j.vetmic.2025.110538 · Cited by 5
Effects of fixatives on histomagnetic evaluation of iron in rodent spleen
Walsh, K. J., Shah, S. V., Wei, P. Y., Oberdick, S. D., Dickson‐Karn, N. M., McTigue, D. M., & Agarwal, G. (2020) · Journal of Magnetism and Magnetic Materials · doi:10.1016/j.jmmm.2020.167531 · Cited by 5
Intracellular transformation and disposal mechanisms of magnetosomes in macrophages and cancer cells
Gandarias, L., Gubieda, A. G., Gorni, G., Mathon, O., Olivi, L., Abad, A., Fdez-Gubieda, M. L., Muela, A., & Garcı́a-Prieto, A. (2023) · Biotechnology Journal · doi:10.1002/biot.202300173 · Cited by 5
Heme and immunity: The heme oxygenase dichotomy
Perry, M., & Hamza, I. (2025) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2025.112844 · Cited by 5
Self-citationMetchnikoff's Legacy: Tissue Phagocytes and Functions
Giacomo, A. D. (2017) · European Journal of Immunology · doi:10.1002/eji.201770016 · Cited by 5
Fu, W., Li, X., Guo, L., Huang, Y., Hong, L., Zhong, L., Li, Z., Lu, B., Fang, Y., Qiu, Z., et al. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.124158 · Cited by 4
A novel process for transcellular hemoglobin transport from macrophages to cancer cells
Braniewska, A., Skorzynski, M., Sas, Z., Długołęcka, M., Marszałek, I., Kurpiel, D., Bühler, M., Strzemecki, D., Karpińska, A., Białasek, M., et al. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01929-8 · Cited by 5
Liu, X., Cai, N., Dai, Y., Chen, X., & Zeng, X. (2025) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2025.1578163 · Cited by 4
Chen, S., Yin, W., Zhi, H., Zhang, X., An, L., Yang, Z., Li, R., Cai, Y., You, C., Li, Y., et al. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.113956 · Cited by 4
Li, Z., Peng, Y., Wang, Q., Zhou, H., & Fu, X. (2026) · ACS Nano Medicine · doi:10.1021/acsnanomed.5c00190 · Cited by 5
Plasma proteomic analysis on neuropathic pain in idiopathic peripheral neuropathy patients
van Doormaal, P. T. C., Thomas, S., Ajroud‐Driss, S., Cole, R. N., Devine, L. R., Dimachkie, M. M., Geisler, S., Freeman, R. L., Simpson, D. M., Singleton, J. R., et al. (2023) · Journal of the Peripheral Nervous System · doi:10.1111/jns.12606 · Cited by 4
Liu, Z.-Z., Wang, H., Zhang, Z., Ma, Y., Jing, Q., Zhang, S., Han, J., Chen, J., Xiang, Y., Kou, Y., et al. (2024) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0012163 · Cited by 4
Shen, M., Guo, Q., Li, W., & Qian, Z. (2024) · Genes and Immunity · doi:10.1038/s41435-024-00290-7 · Cited by 4
Hanna, M., Akabawy, A. M. A., Khalifa, M. M., Elbaset, M. A., Imam, R. A., & Seddiek, H. (2025) · Frontiers in Physiology · doi:10.3389/fphys.2025.1430946 · Cited by 4
Wu, X., Gao, L., Zhou, K., Li, X., Lin, X., Wan, D., Xiong, X., Liu, G., & Yin, Y. (2018) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2018.04.007 · Cited by 4
Identification of a secretory heme‐binding protein from Nocardia seriolae involved in cell apoptosis
Wen, Y., Kang, X., Li, Z., Xia, L., & Lu, Y. (2022) · Journal of Fish Diseases · doi:10.1111/jfd.13654 · Cited by 4
Luo, Q., Zhou, X., Lv, X., Zheng, W., Geng, S., Xu, T., & Sun, Y. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.109147 · Cited by 4
Бородулина, Е. А., & Yakovleva, E. (2020) · Russian Clinical Laboratory Diagnostics · doi:10.18821/0869-2084-2020-65-3-149-154 · Cited by 4
Iron in Cell Metabolism and Disease
Eeka, P. (2022) · Biochemistry · doi:10.5772/intechopen.101908 · Cited by 4
Crisell, D., Talbot, N. P., & Drakesmith, H. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_14 · Cited by 4
Yang, F., Luo, S., Yang, D., Cui, X., Zhang, D., Wang, H., Li, Y., Xie, W., Wang, L., Zhang, X., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1626888 · Cited by 3
An acetylation-dependent switch underlies host disease tolerance during streptococcal infection
Paudel, S. K., Gannavaram, S., Caparon, M. G., & Xu, W. (2026) · Scientific Reports · doi:10.1038/s41598-026-42565-1 · Cited by 3
Moreno‐Navarrete, J. M., Rodrigues, I. G., & Fernández‐Real, J. M. (2025) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-92033-2_17 · Cited by 3
Loss of NR2F6 Protects from Salmonella Typhimurium Infection
Woelk, J., Pfeifhofer‐Obermair, C., Benz, J., Brigo, N., Bamberger, M., Kleiter, A., Hermann, M., Weiß, G., & Hermann‐Kleiter, N. (2025) · Advanced Science · doi:10.1002/advs.202404280 · Cited by 3
Huang, B., Liu, Q., Bai, C.-M. C., Li, C., Wang, C., & Xin, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076175 · Cited by 3
Metadata
- Authors
- Soares, M. P., & Hamza, I.
- Affiliations
- Instituto Gulbenkian de Ciência (PT)
- University of Maryland, College Park (US)
- Corresponding author
- Soares, Miguel P.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2016-03
- Volume
- 44
- Issue
- 3
- Pages
- 492-504
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC4794998
- OpenAlex
- W2298261633
- Cited by
- 401
- References
- 152
- Citations by year
- 2026: 39 · 2025: 47 · 2024: 38 · 2023: 44 · 2022: 50 · 2021: 53 · 2020: 42 · 2019: 31 · 2018: 24 · 2017: 28 · 2016: 4
- FWCI
- 4.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (R01AI067979, R41AI113998)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK085035, R01DK074797)
- National Institute of Environmental Health Sciences (R21ES025661, R33ES025661)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Immunology and Microbiology › Immunology › Immune cells in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
- Keywords
- macrophages, iron metabolism, heme iron, reactive oxygen species, iron regulation, macrophage function
- MeSH terms
- Animals, Heme, Humans, Iron, Macrophages, Protoporphyrins, Reactive Oxygen Species
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
